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Updated: Jun 13, 2026

Novel RNA-Binding Proteins Isolation by the RaPID Methodology
Published on: September 30, 2016
Ribosomal protein S19 binds to its own mRNA with reduced affinity in Diamond-Blackfan anemia
Jens Schuster1, Anne-Sophie Fröjmark, Per Nilsson
1Department of Genetics and Pathology, Uppsala University, The Rudbeck Laboratory, 751 81 Uppsala, Sweden. jens.schuster@genpat.uu.se
Abstract:
Heterozygous mutations in the ribosomal protein S19 (RPS19) gene are associated with Diamond-Blackfan anemia (DBA). The mechanism by which RPS19 mediates anemia are still unclear, as well as the regulation of RPS19 expression. We show herein that RPS19 binds specifically to the 5' untranslated region of its own mRNA with an equilibrium binding constant (K(D)) of 4.1+/-1.9 nM. We investigated the mRNA binding properties of two mutant RPS19 proteins (W52R and R62W) identified in DBA patients. We observed a significant increase in K(D) for both proteins (16.1+/-2.1 and 14.5+/-4.9 nM, respectively), indicating a reduced RNA binding capability (p<0.05). We suggest that the binding of RPS19 to its mRNA has a regulatory function and hypothesize that the weaker RNA binding of mutant rRPS19 may have implications for the pathophysiological mechanisms in DBA.
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